HAX1_RAT
ID HAX1_RAT Reviewed; 278 AA.
AC Q7TSE9; Q5D1N3; Q5D1N4; Q7TSE7; Q7TSE8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=HCLS1-associated protein X-1;
DE AltName: Full=HS1-associating protein X-1;
DE Short=HAX-1;
DE AltName: Full=HS1-binding protein 1;
DE Short=HSP1BP-1;
GN Name=Hax1; Synonyms=Hs1bp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 5 AND 6).
RC STRAIN=Lewis; TISSUE=Testis;
RX PubMed=16516414; DOI=10.1016/j.gene.2005.11.035;
RA Grzybowska E.A., Sarnowska E., Konopinski R., Wilczynska A.,
RA Sarnowski T.J., Siedlecki J.A.;
RT "Identification and expression analysis of alternative splice variants of
RT the rat Hax-1 gene.";
RL Gene 371:84-92(2006).
RN [2]
RP INTERACTION WITH ABCB1; ABCB4; ABCB11 AND CTTN, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=15159385; DOI=10.1074/jbc.m404337200;
RA Ortiz D.F., Moseley J., Calderon G., Swift A.L., Li S., Arias I.M.;
RT "Identification of HAX-1 as a protein that binds bile salt export protein
RT and regulates its abundance in the apical membrane of Madin-Darby canine
RT kidney cells.";
RL J. Biol. Chem. 279:32761-32770(2004).
RN [3]
RP SUBCELLULAR LOCATION, FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=19913549; DOI=10.1016/j.yjmcc.2009.10.028;
RA Yap S.V., Vafiadaki E., Strong J., Kontrogianni-Konstantopoulos A.;
RT "HAX-1: a multifaceted antiapoptotic protein localizing in the mitochondria
RT and the sarcoplasmic reticulum of striated muscle cells.";
RL J. Mol. Cell. Cardiol. 48:1266-1279(2010).
RN [4]
RP ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=23164465; DOI=10.1111/febs.12066;
RA Grzybowska E.A., Zayat V., Konopinski R., Trebinska A., Szwarc M.,
RA Sarnowska E., Macech E., Korczynski J., Knapp A., Siedlecki J.A.;
RT "HAX-1 is a nucleocytoplasmic shuttling protein with a possible role in
RT mRNA processing.";
RL FEBS J. 280:256-272(2013).
CC -!- FUNCTION: Recruits the Arp2/3 complex to the cell cortex and regulates
CC reorganization of the cortical actin cytoskeleton via its interaction
CC with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation
CC of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in
CC the clathrin-mediated endocytosis pathway. May be involved in
CC internalization of ABC transporters such as ABCB11. May inhibit CASP9
CC and CASP3. Promotes cell survival. May regulate intracellular calcium
CC pools. {ECO:0000250|UniProtKB:O00165, ECO:0000269|PubMed:15159385,
CC ECO:0000269|PubMed:19913549}.
CC -!- SUBUNIT: Interacts with ABCB1, ABCB4 and ABCB11 (PubMed:15159385).
CC Directly associates with HCLS1/HS1, through binding to its N-terminal
CC region (By similarity). Interacts with CTTN (PubMed:15159385).
CC Interacts with PKD2. Interacts with GNA13. Interacts with CASP9.
CC Interacts with ITGB6. Interacts with PLN and ATP2A2; these interactions
CC are inhibited by calcium. Interacts with GRB7. Interacts (via C-
CC terminus) with XIAP/BIRC4 (via BIR 2 domain and BIR 3 domain) and this
CC interaction blocks ubiquitination of XIAP/BIRC4. Interacts with TPC2.
CC Interacts with KCNC3. Interacts with XPO1 (By similarity). Interacts
CC with RNF217 (By similarity). {ECO:0000250|UniProtKB:O00165,
CC ECO:0000269|PubMed:15159385}.
CC -!- INTERACTION:
CC Q7TSE9; O70127: Abcb11; NbExp=5; IntAct=EBI-930005, EBI-930036;
CC Q7TSE9; Q08201: Abcb4; NbExp=3; IntAct=EBI-930005, EBI-929988;
CC Q7TSE9; Q6PSM0: Mdr1a; NbExp=2; IntAct=EBI-930005, EBI-930055;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19913549}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:O00165}. Nucleus membrane
CC {ECO:0000250|UniProtKB:O00165}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:15159385}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:O00165}. Cell membrane
CC {ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00165}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum
CC {ECO:0000269|PubMed:19913549}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:O00165}. Cytoplasm
CC {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000250|UniProtKB:O00165}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000250|UniProtKB:O00165}.
CC Note=Predominantly cytoplasmic. Also detected in the nucleus when
CC nuclear export is inhibited, and in response to cellular stress caused
CC by arsenite (in vitro). {ECO:0000250|UniProtKB:O00165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q7TSE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSE9-2; Sequence=VSP_030139;
CC Name=3;
CC IsoId=Q7TSE9-3; Sequence=VSP_030137;
CC Name=5;
CC IsoId=Q7TSE9-5; Sequence=VSP_030138;
CC Name=6;
CC IsoId=Q7TSE9-6; Sequence=VSP_030138, VSP_030139;
CC -!- TISSUE SPECIFICITY: Present in striated muscles (at protein level).
CC {ECO:0000269|PubMed:19913549}.
CC -!- DEVELOPMENTAL STAGE: Abundant in hindlimb and cardiac muscles
CC throughout embryogenesis (at protein level).
CC {ECO:0000269|PubMed:19913549}.
CC -!- SIMILARITY: Belongs to the HAX1 family. {ECO:0000305}.
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DR EMBL; AY291062; AAP44974.1; -; mRNA.
DR EMBL; AY291063; AAP44975.1; -; mRNA.
DR EMBL; AY291064; AAP44976.1; -; mRNA.
DR EMBL; AY919342; AAX18866.1; -; mRNA.
DR EMBL; AY919343; AAX18867.1; -; mRNA.
DR EMBL; DQ286293; ABB91376.1; -; Genomic_DNA.
DR RefSeq; NP_853658.1; NM_181627.2. [Q7TSE9-1]
DR AlphaFoldDB; Q7TSE9; -.
DR IntAct; Q7TSE9; 4.
DR STRING; 10116.ENSRNOP00000064877; -.
DR jPOST; Q7TSE9; -.
DR PaxDb; Q7TSE9; -.
DR PRIDE; Q7TSE9; -.
DR DNASU; 291202; -.
DR Ensembl; ENSRNOT00000071253; ENSRNOP00000067159; ENSRNOG00000045647. [Q7TSE9-3]
DR Ensembl; ENSRNOT00000073599; ENSRNOP00000064877; ENSRNOG00000045647. [Q7TSE9-1]
DR GeneID; 291202; -.
DR KEGG; rno:291202; -.
DR CTD; 10456; -.
DR RGD; 727960; Hax1.
DR eggNOG; ENOG502S0AE; Eukaryota.
DR GeneTree; ENSGT00390000018324; -.
DR InParanoid; Q7TSE9; -.
DR OrthoDB; 1567048at2759; -.
DR PhylomeDB; Q7TSE9; -.
DR PRO; PR:Q7TSE9; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:CACAO.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0019966; F:interleukin-1 binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:RGD.
DR InterPro; IPR017248; HAX-1.
DR PANTHER; PTHR14938; PTHR14938; 1.
DR PIRSF; PIRSF037634; HS1-associating_X-1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Membrane; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome; Sarcoplasmic reticulum.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00165"
FT CHAIN 2..278
FT /note="HCLS1-associated protein X-1"
FT /id="PRO_0000313801"
FT REGION 2..43
FT /note="Required for localization in mitochondria"
FT REGION 15..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..278
FT /note="Involved in HCLS1 binding"
FT /evidence="ECO:0000250"
FT REGION 174..205
FT /note="Involved in CASP9 binding"
FT /evidence="ECO:0000250"
FT REGION 175..246
FT /note="Involved in GNA13 binding"
FT /evidence="ECO:0000250"
FT REGION 182..278
FT /note="Required for localization in sarcoplasmic reticulum"
FT REGION 183..278
FT /note="Involved in PKD2 binding"
FT /evidence="ECO:0000250"
FT REGION 202..244
FT /note="Involved in ATP2A2 binding"
FT /evidence="ECO:0000250"
FT REGION 202..224
FT /note="Involved in PLN binding"
FT /evidence="ECO:0000250"
FT REGION 269..278
FT /note="Required for ITGB6 binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 28..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 126..127
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O00165"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00165"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00165"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16516414"
FT /id="VSP_030138"
FT VAR_SEQ 1..18
FT /note="MSVFDLFRGFFGFPGPRS -> MQQGPERRKQWGSGKEDREQVIG (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16516414"
FT /id="VSP_030137"
FT VAR_SEQ 44..104
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16516414"
FT /id="VSP_030139"
SQ SEQUENCE 278 AA; 31448 MW; 0B49E32FF89CD975 CRC64;
MSVFDLFRGF FGFPGPRSHR DPFFGGMTRD DDDDEDDEEE EDSGAWGRES YAFDGFHPTE
EFGFSFSPRG GMRFHGNFGF DDLVRDFNSI FSEMGAWTLP SHSPELPGPE SETPGVRLRE
GQTLRDSMLK YPDSHQPRIF EGVLESHAKP ESSKPAPDWG SQGPFHRLDD TWPVSPHSRA
REDKDLDSQV SQEGLGPLLQ PQPKSYFKSI SVTKITKPDG TVEEHRTVVD SEGRRETTVT
HQEAHDSSRS DPDPPRSSAL DDPFSILDLL LGRWFRSR
